title: Functional features of TonB energy transduction systems of Acinetobacter baumannii.
abstract: Acinetobacter baumannii is an opportunistic pathogen that causes severe nosocomial infections. Strain ATCC 19606(T) utilizes the siderophore acinetobactin to acquire iron under iron-limiting conditions encountered in the host. Accordingly, the genome of this strain has three tonB genes encoding proteins for energy transduction functions needed for the active transport of nutrients, including iron, through the outer membrane. Phylogenetic analysis indicates that these tonB genes, which are present in the genomes of all sequenced A. baumannii strains, were acquired from different sources. Two of these genes occur as components of tonB-exbB-exbD operons and one as a monocistronic copy; all are actively transcribed in ATCC 19606(T). The abilities of components of these TonB systems to complement the growth defect of Escherichia coli W3110 mutants KP1344 (tonB) and RA1051 (exbBD) under iron-chelated conditions further support the roles of these TonB systems in iron acquisition. Mutagenesis analysis of ATCC 19606(T) tonB1 (subscripted numbers represent different copies of genes or proteins) and tonB2 supports this hypothesis: their inactivation results in growth defects in iron-chelated media, without affecting acinetobactin biosynthesis or the production of the acinetobactin outer membrane receptor protein BauA. In vivo assays using Galleria mellonella show that each TonB protein is involved in, but not essential for, bacterial virulence in this infection model. Furthermore, we observed that TonB2 plays a role in the ability of bacteria to bind to fibronectin and to adhere to A549 cells by uncharacterized mechanisms. Taken together, these results indicate that A. baumannii ATCC 19606(T) produces three independent TonB proteins, which appear to provide the energy-transducing functions needed for iron acquisition and cellular processes that play a role in the virulence of this pathogen.
authors.affiliation: Department of Microbiology, Miami University, Oxford, Ohio, USA.
authors.forename: Daniel L
authors.initials: DL
authors.lastname: Zimbler
authors.forename: Brock A
authors.initials: BA
authors.lastname: Arivett
authors.forename: Amber C
authors.initials: AC
authors.lastname: Beckett
authors.forename: Sharon M
authors.initials: SM
authors.lastname: Menke
authors.forename: Luis A
authors.initials: LA
authors.lastname: Actis
mesh_terms: D040981:Acinetobacter baumannii / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism*; D001693:Biological Transport, Active; D002460:Cell Line; D004735:Energy Transfer; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D005798:Genes, Bacterial; D006801:Humans; D007501:Iron / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D009876:Operon / Q000235:genetics; D010802:Phylogeny; D016415:Sequence Alignment; D014774:Virulence / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C057616:tonB protein, Bacteria; D007501:Iron